In Vitro Assessment of Guanylyl Cyclase Activity of Plant Receptor Kinases
KAUST DepartmentAnalytical Core Lab
Division of Biological & Environmental Science & Engineering, 4700 King Abdullah University of Science and Technology, Thuwal, 23955-6900, , Saudi Arabia
Permanent link to this recordhttp://hdl.handle.net/10754/625598
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AbstractCyclic nucleotides such as 3′,5′-cyclic adenosine monophosphate (cAMP) and 3′,5′-cyclic guanosine monophosphate (cGMP) are increasingly recognized as key signaling molecules in plants, and a growing number of plant mononucleotide cyclases, both adenylate cyclases (ACs) and guanylate cyclases (GCs), have been reported. Catalytically active cytosolic GC domains have been shown to be part of many plant receptor kinases and hence directly linked to plant signaling and downstream cellular responses. Here we detail, firstly, methods to identify and express essential functional GC domains of receptor kinases, and secondly, we describe mass spectrometric methods to quantify cGMP generated by recombinant GCs from receptor kinases in vitro.
CitationRaji M, Gehring C (2017) In Vitro Assessment of Guanylyl Cyclase Activity of Plant Receptor Kinases. Plant Receptor Kinases: 131–140. Available: http://dx.doi.org/10.1007/978-1-4939-7063-6_13.
SponsorsWe are grateful to the KAUST Analytical Core Lab for supporting this project.
PublisherSpringer New York
JournalMethods in Molecular Biology